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Computational insights into the mechanism of porphobilinogen synthase

Erdtman, E.; Bushnell, E.A.; Gauld, J.W.; Eriksson, L.A.; J. Phys. Chem. B 114, 16860-16870 (2010)

Data extracted from this reference:

Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.24
Zn2+
required for catalysis, bound at the active site
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.24
2 5-aminolevulinate
Saccharomyces cerevisiae
-
porphobilinogen + 2 H2O
-
-
?
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.2.1.24
Saccharomyces cerevisiae
-
-
-
Reaction
EC Number
Reaction
Commentary
Organism
4.2.1.24
2 5-aminolevulinate = porphobilinogen + 2 H2O
reaction mechanism involving asymmetric addition and cyclization of two 5-aminolevulinate molecules, modeling, detailed overview. The active site consists of several invariant residues, including two lysyl residues Lys210 and Lys263 that bind the two substrate moieties as Schiff bases, active site structure and substrate binding, overview. The intersubstrate C-N bond is formed first have a rate-limiting barrier that is lower than those in which the intersubstrate C-C bond is formed first
Saccharomyces cerevisiae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.24
2 5-aminolevulinate
-
716012
Saccharomyces cerevisiae
porphobilinogen + 2 H2O
-
-
-
?
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
4.2.1.24
Zn2+
required for catalysis, bound at the active site
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.2.1.24
2 5-aminolevulinate
Saccharomyces cerevisiae
-
porphobilinogen + 2 H2O
-
-
?
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.2.1.24
2 5-aminolevulinate
-
716012
Saccharomyces cerevisiae
porphobilinogen + 2 H2O
-
-
-
?
General Information
EC Number
General Information
Commentary
Organism
4.2.1.24
metabolism
PBGS is a key enzyme in heme biosynthesis
Saccharomyces cerevisiae
4.2.1.24
physiological function
PBGS is a key enzyme in heme biosynthesis that catalyzes the formation of porphobilinogen from two 5-aminolevulinic acid molecules via formation of intersubstrate C-N and C-C bonds
Saccharomyces cerevisiae
General Information (protein specific)
EC Number
General Information
Commentary
Organism
4.2.1.24
metabolism
PBGS is a key enzyme in heme biosynthesis
Saccharomyces cerevisiae
4.2.1.24
physiological function
PBGS is a key enzyme in heme biosynthesis that catalyzes the formation of porphobilinogen from two 5-aminolevulinic acid molecules via formation of intersubstrate C-N and C-C bonds
Saccharomyces cerevisiae